SPR with Biotinylated Human ANGPT2/Angiopoietin-2 Protein 5210

Biotinylated Human ANGPT2/Angiopoietin-2 Protein 5210

$525.00 – $1,750.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Lys275-Phe496

SKU: 5210parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	N-His-Avi
purity	> 95% as determined by Tris-Bis PAGE
background	Angiopoietin-2 (Ang-2; also ANGPT2) is a secreted glycoprotein that plays a complex role in angiogenesis and inflammation. Mature Ang-2 is 478 amino acids in length.Ang2 is widely expressed during development, but it is restricted postnatally to highly angiogenic tissues such as the placenta, ovaries, and uterus. It is particularly abundant in vascular endothelial cells (EC) where it is stored in intracellular Weibel Palade bodies.
molecular weight	The protein has a predicted MW of 28.4 kDa. Due to glycosylation, the protein migrates to 32-37 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Biotinylated Human ANGPT2/Angiopoietin-2 Protein 5210

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Angiopoietin-2 (Ang-2; also ANGPT2) is a secreted glycoprotein that plays a complex role in angiogenesis and inflammation. Mature Ang-2 is 478 amino acids in length.Ang2 is widely expressed during development, but it is restricted postnatally to highly angiogenic tissues such as the placenta, ovaries, and uterus. It is particularly abundant in vascular endothelial cells (EC) where it is stored in intracellular Weibel Palade bodies.
Protein names Angiopoietin-2 (ANG-2)
Gene names ANGPT2,ANGPT2
Mass 9606Da
Function Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1 (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Involved in the regulation of lymphangiogenesis (PubMed:32908006).
Subellular location Secreted .
Structure Interacts with TEK/TIE2, competing for the same binding site as ANGPT1 (PubMed:12427764, PubMed:15284220, PubMed:19223473, PubMed:32908006, PubMed:9204896). Interacts with ITGA5 (PubMed:32908006). Interacts with SVEP1/polydom (By similarity).
Domain Th
Target Relevance information above includes information from UniProt accession: O15123
The UniProt Consortium

Data

SPR with Biotinylated Human ANGPT2/Angiopoietin-2 Protein

Human TIE2, His Tag immobilized on CM5 Chip can bind Biotinylated Human ANGPT2, His Tag with an affinity constant of 2.93 µM as determined in SPR assay (Biacore T200).

ELISA with Biotinylated Human ANGPT2/Angiopoietin-2 Protein

Immobilized Biotinylated Human ANGPT2, His Tag at 1µg/ml (100µl/Well) on the streptavidin precoated plate (5µg/ml). Dose response curve for Anti-ANGPT2 Antibody, hFc Tag with the EC50 of 3.8ng/ml determined by ELISA (QC Test).

SDS-PAGE gel of Biotinylated Human ANGPT2/Angiopoietin-2 Protein

Biotinylated Human ANGPT2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.